scholarly journals Effects of Substitution of Conserved Amino Acid Residues on the Sugar-Binding Property of the Tandem-Repeat 32-kDa Galectin of the Nematode Caenorhabditis elegans.

2001 ◽  
Vol 24 (1) ◽  
pp. 14-18 ◽  
Author(s):  
Yoichiro ARATA ◽  
Miho SEKIGUCHI ◽  
Jun HIRABAYASHI ◽  
Ken-ichi KASAI
Keyword(s):  
Amino Acid ◽  
Caenorhabditis Elegans ◽  
Tandem Repeat ◽  
Binding Property ◽  
Amino Acid Residues ◽  
Nematode Caenorhabditis Elegans ◽  
Sugar Binding

scholarly journals The primary structure of histone H2A from the nematode Caenorhabditis elegans

1987 ◽  
Vol 243 (1) ◽  
pp. 297-300 ◽  
Author(s):  
J R Vanfleteren ◽  
S M Van Bun ◽  
J J Van Beeumen
Keyword(s):  
Amino Acid ◽  
Caenorhabditis Elegans ◽  
Primary Structure ◽  
Amino Acid Residues ◽  
Histone H2a ◽  
Nematode Caenorhabditis Elegans ◽  
Calf Thymus ◽  
N Terminus ◽  
Lysine Residues ◽  
Complete Primary Structure

The complete primary structure of histone H2A from the nematode Caenorhabditis elegans was determined. The amino acid chain consists of 126 amino acid residues and has a blocked N-terminus. By comparison with calf thymus histone H2A, the nematode protein shows five deletions, two insertions and 16 substitutions. Most of the changes occur in the N- and C-terminal regions of the molecule, whereas the central part covering the residues 21-120 is quite well conserved. The lysine residues 5, 8 and 10 were found to be partially acetylated.

scholarly journals The primary structure of cytochrome c from the nematode Caenorhabditis elegans

1990 ◽  
Vol 271 (3) ◽  
pp. 613-620 ◽  
Author(s):  
J R Vanfleteren ◽  
E A I M Evers ◽  
G Van de Werken ◽  
J J Van Beeumen
Keyword(s):  
Amino Acid ◽  
Caenorhabditis Elegans ◽  
Cytochrome C ◽  
Amino Acid Sequences ◽  
Similar Data ◽  
Amino Acid Residues ◽  
Nematode Caenorhabditis Elegans ◽  
Horse Heart Cytochrome ◽  
Human Cytochrome ◽  
Horse Heart Cytochrome C

The complete amino acid sequence of cytochrome c from the nematode Caenorhabditis elegans was determined. The native protein displays the same spectral properties in the oxidized and reduced states as horse heart cytochrome c. The apoprotein consists of 110 amino acid residues and differs from human cytochrome c by 44 substitutions, one internal deletion, five N-terminal additions and two C-terminal additions. One of the substitutions is the replacement of an ‘invariant’ phenylalanine residue at position 15 by tyrosine. The N-terminal sequence extension contains a short peptide motif, which is highly homologous with a peptide fragment present at the N-terminus of annelid and insect cytochrome c sequences. From the number of amino acid changes and the evolutionary rate of cytochrome c it would appear that nematodes diverged from a line leading to man about 1.4 billion years ago. When similar data based on the amino acid sequences of the histones H1, H2A, H2B and H3 are taken into account, the average estimate is 1.1 +/- 0.1 billion years.

scholarly journals Multiple forms of histone H2B from the nematode Caenorhabditis elegans

1986 ◽  
Vol 235 (3) ◽  
pp. 769-773 ◽  
Author(s):  
J R Vanfleteren ◽  
S M Van Bun ◽  
L L Delcambe ◽  
J J Van Beeumen
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Caenorhabditis Elegans ◽  
Amino Acid Sequence ◽  
Length Polymorphism ◽  
Polypeptide Chain ◽  
Multiple Forms ◽  
Nematode Caenorhabditis Elegans ◽  
Histone H2b ◽  
High Degree

The complete amino acid sequence of histone H2B from the nematode Caenorhabditis elegans was determined. The protein as obtained by us is a mixture of multiple forms. Approx. 90% of the molecules consist of a polypeptide chain of 122 amino acids with alanine as N-terminal residue and proline at the second position. In the remaining 10% alanine is lacking and the chain starts with proline. In addition to the heterogeneity of chain length, polymorphism occurs at the positions 7 (Ala/Lys), 14 (Ala/Lys) and 72 (Ala/Ser) of the major chain and at position 6 (Ala/Lys) of the shorter chain. In the N-terminal third of the molecule there is a high degree of sequence homology to the corresponding region in H2B from Drosophila (insect), Patella (mollusc) and Asterias (starfish). In contrast, this part of the molecule differs considerably from mammalian histone H2B.

scholarly journals The Caenorhabditis elegans unc-13 gene product is a phospholipid-dependent high-affinity phorbol ester receptor

1992 ◽  
Vol 287 (3) ◽  
pp. 995-999 ◽  
Author(s):  
S Ahmed ◽  
I N Maruyama ◽  
R Kozma ◽  
J Lee ◽  
S Brenner ◽  
...  
Keyword(s):  
Amino Acid ◽  
Caenorhabditis Elegans ◽  
Phorbol Ester ◽  
Catalytic Domain ◽  
Amino Acid Residues ◽  
C Elegans ◽  
High Affinity ◽  
Cell Extracts ◽  
Neuronal Connections ◽  
Phorbol Ester Receptor

The Caenorhabditis elegans unc-13 mutant is a member of a class of mutants that have un-coordinated movement. Mutations of the unc-13 gene cause diverse defects in C. elegans, including abnormal neuronal connections and modified synaptic transmission in the nervous system. unc-13 cDNA encodes a protein (UNC-13) of 1734 amino acid residues with a predicted molecular mass of 198 kDa and sequence identity to the C1/C2 regions but not to the catalytic domain of the ubiquitously expressed protein kinase C family [Maruyama & Brenner (1991) Proc. Natl. Acad. Sci. U.S.A. 88, 5729-5733]. To characterize the phorbol ester binding site of the UNC-13 protein, cDNA encoding the C1/C2-like regions (amino acid residues 546-940) was expressed in Escherichia coli and the 43 kDa recombinant protein was purified. Phorbol ester binding to the 43 kDa protein was zinc- and phospholipid-dependent, stereospecific and of high affinity (Kd 67 nM). UNC-13 specific antisera detected a protein of approx. 190 kDa in wild-type (N2) but not in mutant (e1019) C. elegans cell extracts. We conclude that UNC-13 represents a novel class of phorbol ester receptor.

scholarly journals The primary structure of a minor isoform (H1.2) of histone H1 from the nematode Caenorhabditis elegans

1990 ◽  
Vol 265 (3) ◽  
pp. 739-746 ◽  
Author(s):  
J R Vanfleteren ◽  
S M Van Bun ◽  
I De Baere ◽  
J J Van Beeumen
Keyword(s):  
Amino Acid ◽  
Caenorhabditis Elegans ◽  
Secondary Structure ◽  
Alpha Helix ◽  
Histone H1 ◽  
Globular Domain ◽  
Nematode Caenorhabditis Elegans ◽  
Terminal Domain ◽  
Helix Formation ◽  
A Minor

The complete amino acid sequence of a minor isoform (H1.2) of histone H1 from the nematode Caenorhabditis elegans was determined. The amino acid chain consists of 190 residues and has a blocked N-terminus. Histone subtype H1.2 is 17 residues shorter than the major isoform H1.1, mainly as the result of deletions of short peptide fragments. Considerable divergence from isoform H1.1 has occurred in the N-terminal domain and the very C-terminus of the molecule, but the central globular domain and most of the C-terminal domain, including two potential phosphorylation sites, have been well conserved. Secondary-structure predictions for both H1 isoforms reveal a high potential for helix formation in the N-terminal region 1-33 of isoform H1.1 whereas the corresponding region in isoform H1.2 has low probability of being found in alpha-helix. No major differences in secondary structure are predicted for other parts of both H1 subtypes. The aberrant conformation of isoform H1.2 may be indicative of a significantly different function.

scholarly journals C-terminal Amino Acid Residues Are Required for the Folding and Cholesterol Binding Property of Perfringolysin O, a Pore-forming Cytolysin

1999 ◽  
Vol 274 (26) ◽  
pp. 18536-18542 ◽  
Author(s):  
Yukiko Shimada ◽  
Megumi Nakamura ◽  
Yasuhide Naito ◽  
Kohji Nomura ◽  
Yoshiko Ohno-Iwashita
Keyword(s):  
Amino Acid ◽  
Binding Property ◽  
Amino Acid Residues ◽  
Terminal Amino Acid ◽  
Perfringolysin O ◽  
Terminal Amino ◽  
Cholesterol Binding
Sign in / Sign up

Export Citation Format

Share Document